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Anne's paper on Easy Expression and Purification of Fluorescent N-Terminal BCL11B CCHC Zinc Finger Domain is published

(A) BCL11B42-94 fusion protein sequence showing an N-terminal His6-tag, fluorescent CyPet, and mEYFP protein tag, respectively, a flexible linker region, a TEV-cleaving site, enzyme restriction sites XhoI and KpnI, and the BCL11B42-94 zinc finger domain. The BCL11B42-94 domain has a size of 5.5 kDa, and the full-length fluorescent fusion proteins have a size of 36 kDa each. (B) SDS-PAGE showing expression trials of CyPet- and mEYFP-BCL11B42-94 in E. coli NiCo21 grown in TB medium at 37 °C at different time points or (C) at 16 °C overnight. For comparative reasons, all E. coli cultures were diluted to an OD600 = 0.6 before lysis and loading the gel.
Purification of CyPet-BCL11B42-94. (A) Chromatogram of CyPet-BCL11B42-94 purification using IMAC. (B) Corresponding SDS-PAGE showing the collected fractions. The flow-through (black) shows E. coli proteins that do not bind to the column. The wash (red) contains loosely bound proteins. The wash step with 5% elution buffer (blue) is crucial to obtain the highly pure fluorescently tagged zinc finger domain (yellow). (C) Purified CyPet-BCL11B42-94 under UV light.

Easy and fast preparation protocol to highly yield the fluorescently tagged protein of the recombinant N-terminal BCL11B zinc finger domain (BCL11B42-94) ...

Anne's paper on Easy Expression and Purification of Fluorescent N-Terminal BCL11B CCHC Zinc Finger Domain is published in Molecules. Congratulations Anne!

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